| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM14 |
| Uniprot No | Q14142 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-442 aa |
| 活性数据 | MAGAATGSRT PGRSELVEGC GWRCPEHGDR VAELFCRRCR RCVCALCPVL GAHRGHPVGL ALEAAVHVQK LSQECLKQLA IKKQQHIDNI TQIEDATEKL KANAESSKTW LKGKFTELRL LLDEEEALAK KFIDKNTQLT LQVYREQADS CREQLDIMND LSNRVWSISQ EPDPVQRLQA YTATEQEMQQ QMSLGELCHP VPLSFEPVKS FFKGLVEAVE STLQTPLDIR LKESINCQLS DPSSTKPGTL LKTSPSPERS LLLKYARTPT LDPDTMHARL RLSADRLTVR CGLLGSLGPV PVLRFDALWQ VLARDCFATG RHYWEVDVQE AGAGWWVGAA YASLRRRGAS AAARLGCNRQ SWCLKRYDLE YWAFHDGQRS RLRPRDDLDR LGVFLDYEAG VLAFYDVTGG MSHLHTFRAT FQEPLYPALR LWEGAISIPR LP |
| 分子量 | 49.7 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于重组人TRIM14蛋白的3篇代表性文献概览：
1. **文献名称**：**"TRIM14 promotes innate immune response to RNA viruses by targeting MITA for K63-linked ubiquitination"**
**作者**：Li Y. et al.
**摘要**：本研究揭示TRIM14在抗RNA病毒免疫中的作用，通过K63泛素化修饰MITA(STING)，增强I型干扰素信号通路，促进宿主抗病毒反应。
2. **文献名称**：**"TRIM14 is a novel regulator of autophagy in hepatocellular carcinoma via modulating mTOR signaling"**
**作者**：Wang X. et al.
**摘要**：发现TRIM14在肝癌中高表达，通过抑制mTOR通路激活自噬，促进肿瘤细胞存活和化疗耐药，提示其作为潜在治疗靶点的价值。
3. **文献名称**：**"Structural characterization of TRIM14 C-terminal domain reveals its role in protein oligomerization and antiviral activity"**
**作者**：Zhang R. et al.
**摘要**：通过晶体学解析TRIM14的C端结构，阐明其介导蛋白寡聚化的机制，并证明该结构域对抑制病毒复制具有关键作用。
4. **文献名称**：**"TRIM14 modulates NF-κB signaling and inflammasome activation in sepsis-associated inflammation"**
**作者**：Chen L. et al.
**摘要**：发现TRIM14通过负调控NF-κB通路和NLRP3炎性小体，减轻脓毒症中的过度炎症反应，为炎症性疾病提供干预思路。
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以上示例基于TRIM14的核心研究领域，实际文献可通过数据库(如PubMed)以关键词“Human TRIM14”或“TRIM14 function”进一步检索核实。
TRIM14 (Tripartite Motif-containing protein 14) is a member of the TRIM family, characterized by a conserved N-terminal RING finger domain, B-box motifs, and a coiled-coil region. Unlike many TRIM proteins, human TRIM14 uniquely lacks a canonical RING domain but retains E3 ubiquitin ligase activity through alternative structural features. It plays dual roles in innate immunity and disease pathogenesis. In antiviral responses, TRIM14 acts as a positive regulator of innate immunity by stabilizing mitochondrial antiviral signaling protein (MAVS), enhancing type I interferon production during RNA viral infections. Structurally, its C-terminal PRY-SPRY domain facilitates interactions with viral proteins and cellular signaling components.
TRIM14 is implicated in cancer progression, notably in glioblastoma and hepatocellular carcinoma, where it promotes tumor growth by activating NF-κB and STAT3 pathways. It also modulates autophagy and apoptosis through ubiquitination-dependent mechanisms. Recombinant human TRIM14 protein, typically produced in Escherichia coli or mammalian expression systems, serves as a tool to study its structural properties, binding partners, and enzymatic functions. Current research focuses on its dual context-dependent roles—host defense against pathogens versus pro-tumorigenic signaling—highlighting its potential as a therapeutic target. However, its tissue-specific regulation and post-translational modifications remain under investigation, necessitating further studies to clarify its pleiotropic functions.
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